Structural diversity of calmodulin binding to its target sites
Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the l...
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| Published in | The FEBS journal Vol. 280; no. 21; pp. 5551 - 5565 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
England
Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
01.11.2013
Blackwell Publishing Ltd |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1742-464X 1742-4658 1742-4658 |
| DOI | 10.1111/febs.12296 |
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| Abstract | Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM‐complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM‐binding sites and mechanisms, such as those for CaM‐activated protein kinases and phosphatases, voltage‐gated Ca²⁺‐channels and the plasma membrane Ca²⁺‐ATPase. |
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| AbstractList | Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca(2+)-channels and the plasma membrane Ca(2+)-ATPase.Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca(2+)-channels and the plasma membrane Ca(2+)-ATPase. Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca2+-channels and the plasma membrane Ca2+-ATPase. Canonical binding mode observed in selected CaM-complex structures. (A) Myosin light chain kinase. (B) CaM-dependent protein kinase II. (C) CaM-dependent protein kinase kinase. (D) Ryanodine receptor. (E) Vacuolar Ca2+-ATPase. (F) Nitric oxide synthase. The spacing of hydrophobic anchor residues is indicated. CaM is coloured cyan with residues forming hydrophobic pocket in olive. The target peptides are coloured grey with anchor residues in red. Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM‐complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM‐binding sites and mechanisms, such as those for CaM‐activated protein kinases and phosphatases, voltage‐gated Ca 2+ ‐channels and the plasma membrane Ca 2+ ‐ ATP ase. Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM‐complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM‐binding sites and mechanisms, such as those for CaM‐activated protein kinases and phosphatases, voltage‐gated Ca²⁺‐channels and the plasma membrane Ca²⁺‐ATPase. Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca(2+)-channels and the plasma membrane Ca(2+)-ATPase. Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca2+-channels and the plasma membrane Ca2+-ATPase. Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM‐complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM‐binding sites and mechanisms, such as those for CaM‐activated protein kinases and phosphatases, voltage‐gated Ca2+‐channels and the plasma membrane Ca2+‐ATPase. Canonical binding mode observed in selected CaM‐complex structures. (A) Myosin light chain kinase. (B) CaM‐dependent protein kinase II. (C) CaM‐dependent protein kinase kinase. (D) Ryanodine receptor. (E) Vacuolar Ca2+‐ATPase. (F) Nitric oxide synthase. The spacing of hydrophobic anchor residues is indicated. CaM is coloured cyan with residues forming hydrophobic pocket in olive. The target peptides are coloured grey with anchor residues in red. |
| Author | Tidow, Henning Nissen, Poul |
| Author_xml | – sequence: 1 fullname: Tidow, Henning – sequence: 2 fullname: Nissen, Poul |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23601118$$D View this record in MEDLINE/PubMed |
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| Issue | 21 |
| Keywords | calcium calmodulin calmodulin-binding site EF-hands ion channels |
| Language | English |
| License | 2013 FEBS. |
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| SubjectTerms | Animals apoptosis Binding Sites Ca2-transporting ATPase calcium Calcium - metabolism calmodulin Calmodulin - chemistry Calmodulin - metabolism calmodulin‐binding site EF‐hands Humans immune response inflammation ion channels Kinases memory metabolism Models, Molecular muscle contraction Myosin-Light-Chain Kinase - metabolism nuclear magnetic resonance spectroscopy Olea plasma membrane plasma membranes Protein Binding protein kinase protein kinases Proteins |
| Title | Structural diversity of calmodulin binding to its target sites |
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